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UniProtKB/Swiss-Prot entry P50362


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G3PA_CHLRE
Primary accession number P50362
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 69)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic [Precursor]
Synonyms EC 1.2.1.13
NADP-dependent glyceraldehydephosphate dehydrogenase subunit A
Gene name
Name: GAPA
From
Chlamydomonas reinhardtii [TaxID: 3055] 
Taxonomy Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1132;
DOI=10.1038/367387a0; PubMed=8114942 [NCBI, ExPASy, EBI, Israel, Japan]
Kersanach R., Brinkmann H., Liaud M.-F., Zhang D.-X., Martin W., Cerff R.;
"Five identical intron positions in ancient duplicated genes of eubacterial origin.";
Nature 367:387-389(1994).
[2]
SUBUNIT, AND INTERACTION WITH CP12.
DOI=10.1021/bi034474x; PubMed=12846565 [NCBI, ExPASy, EBI, Israel, Japan]
Graciet E., Gans P., Wedel N., Lebreton S., Camadro J.-M., Gontero B.;
"The small protein CP12: a protein linker for supramolecular complex assembly.";
Biochemistry 42:8163-8170(2003).
[3]
INTERACTION WITH CP12.
DOI=10.1046/j.1432-1033.2003.03372.x; PubMed=12492483 [NCBI, ExPASy, EBI, Israel, Japan]
Graciet E., Lebreton S., Camadro J.-M., Gontero B.;
"Characterization of native and recombinant A4 glyceraldehyde 3-phosphate dehydrogenase. Kinetic evidence for conformation changes upon association with the small protein CP12.";
Eur. J. Biochem. 270:129-136(2003).
[4]
3D-STRUCTURE MODELING OF 35-374.
Li A.D., Stevens F.J., Huppe H.C., Kersanach R., Anderson L.E.;
"Chlamydomonas reinhardtii NADP-linked glyceraldehyde-3-phosphate dehydrogenase contains the cysteine residues identified as potentially domain-locking in the higher plant enzyme and is light activated.";
Photosyn. Res. 51:167-177(1997).
Comments
  • CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH.
  • PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
  • SUBUNIT: Homotetramer. Component of a complex that contains two dimers of PRK, two tetramers of GAPDH and CP12. CP12 associates with GAPDH, causing its conformation to change. This GAPDH/CP12 complex binds PRK to form a half-complex (one unit). This unit probably dimerizes due partially to interactions between the enzymes of each unit.
  • SUBCELLULAR LOCATION: Plastid, chloroplast.
  • MISCELLANEOUS: GAPDHB, the second subunit found in plants, is absent in algae.
  • MISCELLANEOUS: Algae contain three forms of GAPDH: two cytosolic forms which participate in glycolysis and one chloroplastic form which participates in photosynthesis. These three forms are encoded by distinct genes.
  • SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L27668; AAA86855.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T07990; T07990.
RefSeq XP_001689871.1; -.
UniGene Cre.2829
3D structure databases
PDB
1NLG; Model; -; A=35-374.[ExPASy / RCSB / EBI]
1NLH; Model; -; A=35-374.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NLG; -.
1NLH; -.
SMR P50362; 37-372.
ModBase P50362.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P50362.
Genome annotation databases
GeneID 5715019; -.
KEGG cre:CHLREDRAFT_129019; -.
Other
ProtoNet P50362.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    34  34     Chloroplast (By similarity). 
CHAIN   35   374  340     Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic. PRO_0000010418
NP_BIND   47    48  2     NADP (By similarity). 
REGION   189   191  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   248   249  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   190   190        Nucleophile (By similarity). 
BINDING   71    71        NADP (By similarity). 
BINDING   116   116        NADP; via carbonyl oxygen (By similarity). 
BINDING   220   220        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   235   235        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   271   271        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   353   353        NADP (By similarity). 
SITE   217   217  1     Activates thiol group during catalysis (By similarity). 
DISULFID   55   325        By similarity. 
STRAND   37    43  7      
TURN   45    47  3      
HELIX   48    54  7      
TURN   55    59  5      
STRAND   64    73  10      
HELIX   75    83  9      
TURN   86    88  3      
STRAND   100   104  5      
TURN   124   127  4      
STRAND   129   133  5      
STRAND   135   137  3      
HELIX   141   144  4      
HELIX   146   151  6      
STRAND   153   160  8      
TURN   171   173  3      
STRAND   174   177  4      
STRAND   184   186  3      
HELIX   190   205  16      
STRAND   208   217  10      
STRAND   220   223  4      
STRAND   225   227  3      
HELIX   233   236  4      
TURN   239   241  3      
STRAND   244   246  3      
HELIX   250   257  8      
STRAND   262   271  10      
STRAND   278   290  13      
HELIX   294   302  9      
TURN   303   310  8      
STRAND   311   316  6      
HELIX   321   323  3      
STRAND   327   333  7      
TURN   334   336  3      
STRAND   341   351  11      
HELIX   355   371  17      
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 40304 Da [This is the MW of the unprocessed precursor] CRC64: 8CEB02897930D34C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAAMMQKSAF TGSAVSSKSG VRAKAARAVV DVRAEKKIRV AINGFGRIGR NFLRCWHGRQ 

        70         80         90        100        110        120 
NTLLDVVAIN DSGGVKQASH LLKYDSTLGT FAADVKIVDD SHISVDGKQI KIVSSRDPLQ 

       130        140        150        160        170        180 
LPWKEMNIDL VIEGTGVFID KVGAGKHIQA GASKVLITAP AKDKDIPTFV VGVNEGDYKH 

       190        200        210        220        230        240 
EYPIISNASC TTNCLAPFVK VLEQKFGIVK GTMTTTHSYT GDQRLLDASH RDLRRARAAA 

       250        260        270        280        290        300 
LNIVPTTTGA AKAVSLVLPS LKGKLNGIAL RVPTPTVSVV DLVVQVEKKT FAEEVNAAFR 

       310        320        330        340        350        360 
EAANGPMKGV LHVEDAPLVS IDFKCTDQST SIDASLTMVM GDDMVKVVAW YDNEWGYSQR 

       370 
VVDLAEVTAK KWVA 

P50362 in FASTA format

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